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Volumn 34, Issue 4, 2014, Pages 311-320

The carbohydrate-binding domain of overexpressed STBD1 is important for its stability and protein-protein interactions

Author keywords

CBM20; Endoplasmic reticulum; Glucose; Glycogen; STBD1; Ubiquitination

Indexed keywords

CARBOHYDRATE; GLYCOGEN; MEMBRANE PROTEIN; PROTEASOME; TRYPTOPHAN;

EID: 84906833059     PISSN: 01448463     EISSN: 15734935     Source Type: Journal    
DOI: 10.1042/BSR20140053     Document Type: Article
Times cited : (25)

References (38)
  • 1
    • 0032213808 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of a novel human gene encoding two 41-43 kDa skeletal muscle internal membrane proteins
    • Bouju, S., Lignon, M. F., Pietu, G., Le Cunff, M., Leger, J. J. and Dechesne, C. A. (1998) Molecular cloning and functional expression of a novel human gene encoding two 41-43 kDa skeletal muscle internal membrane proteins. Biochem. J. 335, 549-556 PubMed (Pubitemid 28515407)
    • (1998) Biochemical Journal , vol.335 , Issue.3 , pp. 549-556
    • Bouju, S.1    Lignon, M.-F.2    Pietu, G.3    Le, C.M.4    Leger, J.-J.5    Auffray, C.6    Dechesne, C.A.7
  • 3
    • 69449083006 scopus 로고    scopus 로고
    • The carbohydrate-binding module family 20: Diversity, structure, and function
    • CrossRef PubMed
    • Christiansen, C., Abou Hachem, M., Janecek, S., Vikso-Nielsen, A., Blennow, A. and Svensson, B. (2009) The carbohydrate-binding module family 20: diversity, structure, and function. FEBS J. 276, 5006-5029 CrossRef PubMed
    • (2009) FEBS J. , vol.276 , pp. 5006-5029
    • Christiansen, C.1    Abou Hachem, M.2    Janecek, S.3    Vikso-Nielsen, A.4    Blennow, A.5    Svensson, B.6
  • 4
    • 80054683038 scopus 로고    scopus 로고
    • Structural and evolutionary aspects of two families of non-catalytic domains present in starch and glycogen binding proteins from microbes, plants and animals
    • CrossRef PubMed
    • Janecek, S., Svensson, B. and MacGregor, E. A. (2011) Structural and evolutionary aspects of two families of non-catalytic domains present in starch and glycogen binding proteins from microbes, plants and animals. Enzyme Microb. Technol. 49, 429-440 CrossRef PubMed
    • (2011) Enzyme Microb. Technol. , vol.49 , pp. 429-440
    • Janecek, S.1    Svensson, B.2    MacGregor, E.A.3
  • 7
    • 84885543075 scopus 로고    scopus 로고
    • Myocardial glycophagy-a specific glycogen handling response to metabolic stress is accentuated in the female heart
    • CrossRef PubMed
    • Reichelt, M. E., Mellor, K. M., Curl, C. L., Stapleton, D. and Delbridge, L. M. (2013) Myocardial glycophagy-a specific glycogen handling response to metabolic stress is accentuated in the female heart. J. Mol. Cell. Cardiol. 65, 67-75 CrossRef PubMed
    • (2013) J. Mol. Cell. Cardiol. , vol.65 , pp. 67-75
    • Reichelt, M.E.1    Mellor, K.M.2    Curl, C.L.3    Stapleton, D.4    Delbridge, L.M.5
  • 8
    • 84900822951 scopus 로고    scopus 로고
    • Cardiomyocyte glycophagy is regulated by insulin and exposure to high extracellular glucose
    • CrossRef PubMed
    • Mellor, K. M., Varma, U., Stapleton, D. I. and Delbridge, L. M. (2014) Cardiomyocyte glycophagy is regulated by insulin and exposure to high extracellular glucose. Am. J. Physiol. Heart Circ. Physiol. 306, H1240-H1245 CrossRef PubMed
    • (2014) Am. J. Physiol. Heart Circ. Physiol. , vol.306
    • Mellor, K.M.1    Varma, U.2    Stapleton, D.I.3    Delbridge, L.M.4
  • 9
    • 79960878784 scopus 로고    scopus 로고
    • Atg8: An autophagy-related ubiquitin-like protein family
    • CrossRef PubMed
    • Shpilka, T., Weidberg, H., Pietrokovski, S. and Elazar, Z. (2011) Atg8: an autophagy-related ubiquitin-like protein family. Genome Biol. 12, 226 CrossRef PubMed
    • (2011) Genome Biol. , vol.12 , pp. 226
    • Shpilka, T.1    Weidberg, H.2    Pietrokovski, S.3    Elazar, Z.4
  • 11
    • 84891372222 scopus 로고    scopus 로고
    • Stbd1 is highly elevated in skeletal muscle of Pompe disease mice but suppression of its expression does not affect lysosomal glycogen accumulation
    • CrossRef PubMed
    • Yi, H., Fredrickson, K. B., Das, S., Kishnani, P. S. and Sun, B. (2013) Stbd1 is highly elevated in skeletal muscle of Pompe disease mice but suppression of its expression does not affect lysosomal glycogen accumulation. Mol. Genet. Metab. 109, 312-314 CrossRef PubMed
    • (2013) Mol. Genet. Metab. , vol.109 , pp. 312-314
    • Yi, H.1    Fredrickson, K.B.2    Das, S.3    Kishnani, P.S.4    Sun, B.5
  • 12
    • 34948889895 scopus 로고    scopus 로고
    • A role for AGL ubiquitination in the glycogen storage disorders of Lafora and Cori's disease
    • DOI 10.1101/gad.1553207
    • Cheng, A., Zhang, M., Gentry, M. S., Worby, C. A., Dixon, J. E. and Saltiel, A. R. (2007) A role for AGL ubiquitination in the glycogen storage disorders of Lafora and Cori's disease. Genes Dev. 21, 2399-2409 CrossRef PubMed (Pubitemid 47529370)
    • (2007) Genes and Development , vol.21 , Issue.19 , pp. 2399-2409
    • Cheng, A.1    Zhang, M.2    Gentry, M.S.3    Worby, C.A.4    Dixon, J.E.5    Saltiel, A.R.6
  • 13
    • 65549088453 scopus 로고    scopus 로고
    • Distinct mutations in the glycogen debranching enzyme found in glycogen storage disease type III lead to impairment in diverse cellular functions
    • CrossRef PubMed
    • Cheng, A., Zhang, M., Okubo, M., Omichi, K. and Saltiel, A. R. (2009) Distinct mutations in the glycogen debranching enzyme found in glycogen storage disease type III lead to impairment in diverse cellular functions. Hum. Mol. Genet. 18, 2045-2052 CrossRef PubMed
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 2045-2052
    • Cheng, A.1    Zhang, M.2    Okubo, M.3    Omichi, K.4    Saltiel, A.R.5
  • 14
    • 0033450497 scopus 로고    scopus 로고
    • Glycogen storage disease type IIIa: First report of a causative missense mutation (G1448R) of the glycogen debranching enzyme gene found in a homozygous patient
    • CrossRef PubMed
    • Okubo, M., Kanda, F., Horinishi, A., Takahashi, K., Okuda, S., Chihara, K. and Murase, T. (1999) Glycogen storage disease type IIIa: first report of a causative missense mutation (G1448R) of the glycogen debranching enzyme gene found in a homozygous patient. Hum. Mutat. 14, 542-543 CrossRef PubMed
    • (1999) Hum. Mutat. , vol.14 , pp. 542-543
    • Okubo, M.1    Kanda, F.2    Horinishi, A.3    Takahashi, K.4    Okuda, S.5    Chihara, K.6    Murase, T.7
  • 15
    • 0036079985 scopus 로고    scopus 로고
    • Molecular characterization of glycogen storage disease type III
    • CrossRef PubMed
    • Shen, J. J. and Chen, Y. T. (2002) Molecular characterization of glycogen storage disease type III. Curr. Mol. Med. 2, 167-175 CrossRef PubMed
    • (2002) Curr. Mol. Med. , vol.2 , pp. 167-175
    • Shen, J.J.1    Chen, Y.T.2
  • 16
    • 84872791269 scopus 로고    scopus 로고
    • Laforin, a protein with many faces: Glucan phosphatase, adapter protein, et al
    • CrossRef PubMed
    • Gentry, M. S., Roma-Mateo, C. and Sanz, P. (2013) Laforin, a protein with many faces: glucan phosphatase, adapter protein, et al. FEBS J. 280, 525-537 CrossRef PubMed
    • (2013) FEBS J. , vol.280 , pp. 525-537
    • Gentry, M.S.1    Roma-Mateo, C.2    Sanz, P.3
  • 17
    • 80054056849 scopus 로고    scopus 로고
    • Are there errors in glycogen biosynthesis and is Laforin a repair enzyme?
    • CrossRef PubMed
    • Roach, P. J. (2011) Are there errors in glycogen biosynthesis and is Laforin a repair enzyme? FEBS Lett. 585, 3216-3218 CrossRef PubMed
    • (2011) FEBS Lett. , vol.585 , pp. 3216-3218
    • Roach, P.J.1
  • 20
    • 33846025444 scopus 로고    scopus 로고
    • Dimerization of Laforin is required for its optimal phosphatase activity, regulation of GSK3beta phosphorylation, and Wnt signaling
    • DOI 10.1074/jbc.M607778200
    • Liu, Y., Wang, Y., Wu, C. and Zheng, P. (2006) Dimerization of Laforin is required for its optimal phosphatase activity, regulation of GSK3beta phosphorylation, and Wnt signaling. J. Biol. Chem. 281, 34768-34774 CrossRef PubMed (Pubitemid 46043246)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.46 , pp. 34768-34774
    • Liu, Y.1    Wang, Y.2    Wu, C.3    Liu, Y.4    Zheng, P.5
  • 21
    • 80052048669 scopus 로고    scopus 로고
    • Laforin, a dual specificity phosphatase involved in Lafora disease, is present mainly as monomeric form with full phosphatase activity
    • CrossRef PubMed
    • Dukhande, V. V., Rogers, D. M., Roma-Mateo, C., Donderis, J., Marina, A., Taylor, A. O., Sanz, P. and Gentry, M. S. (2011) Laforin, a dual specificity phosphatase involved in Lafora disease, is present mainly as monomeric form with full phosphatase activity. PLoS ONE 6, e24040 CrossRef PubMed
    • (2011) PLoS ONE , vol.6
    • Dukhande, V.V.1    Rogers, D.M.2    Roma-Mateo, C.3    Donderis, J.4    Marina, A.5    Taylor, A.O.6    Sanz, P.7    Gentry, M.S.8
  • 22
    • 27744464555 scopus 로고    scopus 로고
    • Changes in integrin expression during adipocyte differentiation
    • CrossRef PubMed
    • Liu, J., DeYoung, S. M., Zhang, M., Cheng, A. and Saltiel, A. R. (2005) Changes in integrin expression during adipocyte differentiation. Cell Metab. 2, 165-177 CrossRef PubMed
    • (2005) Cell Metab. , vol.2 , pp. 165-177
    • Liu, J.1    DeYoung, S.M.2    Zhang, M.3    Cheng, A.4    Saltiel, A.R.5
  • 23
    • 20844463813 scopus 로고    scopus 로고
    • Insights into Lafora disease: Malin is an E3 ubiquitin ligase that ubiquitinates and promotes the degradation of laforin
    • DOI 10.1073/pnas.0503285102
    • Gentry, M. S., Worby, C. A. and Dixon, J. E. (2005) Insights into Lafora disease: malin is an E3 ubiquitin ligase that ubiquitinates and promotes the degradation of Laforin. Proc. Natl. Acad. Sci. U.S.A. 102, 8501-8506 CrossRef PubMed (Pubitemid 40862765)
    • (2005) Proceedings of the National Academy of Sciences of the United States of America , vol.102 , Issue.24 , pp. 8501-8506
    • Gentry, M.S.1    Worby, C.A.2    Dixon, J.E.3
  • 24
    • 33751103910 scopus 로고    scopus 로고
    • CAP interacts with cytoskeletal proteins and regulates adhesion-mediated ERK activation and motility
    • DOI 10.1038/sj.emboj.7601406, PII 7601406
    • Zhang, M., Liu, J., Cheng, A., Deyoung, S. M., Chen, X., Dold, L. H. and Saltiel, A. R. (2006) CAP interacts with cytoskeletal proteins and regulates adhesion-mediated ERK activation and motility. EMBO J. 25, 5284-5293 CrossRef PubMed (Pubitemid 44764138)
    • (2006) EMBO Journal , vol.25 , Issue.22 , pp. 5284-5293
    • Zhang, M.1    Liu, J.2    Cheng, A.3    DeYoung, S.M.4    Chen, X.5    Dold, L.H.6    Saltiel, A.R.7
  • 25
    • 0034714239 scopus 로고    scopus 로고
    • Glycogen synthase association with the striated muscle glycogen-targeting subunit of protein phosphatase-1. Synthase activation involves scaffolding regulated by beta-adrenergic signaling
    • CrossRef PubMed
    • Liu, J. and Brautigan, D. L. (2000) Glycogen synthase association with the striated muscle glycogen-targeting subunit of protein phosphatase-1. Synthase activation involves scaffolding regulated by beta-adrenergic signaling. J. Biol. Chem. 275, 26074-26081 CrossRef PubMed
    • (2000) J. Biol. Chem. , vol.275 , pp. 26074-26081
    • Liu, J.1    Brautigan, D.L.2
  • 26
    • 80053338210 scopus 로고    scopus 로고
    • Starch-binding domain-containing protein 1 (Stbd1) and glycogen metabolism: Identification of the Atg8 family interacting motif (AIM) in Stbd1 required for interaction with GABARAPL1
    • CrossRef PubMed
    • Jiang, S., Wells, C. D. and Roach, P. J. (2011) Starch-binding domain-containing protein 1 (Stbd1) and glycogen metabolism: identification of the Atg8 family interacting motif (AIM) in Stbd1 required for interaction with GABARAPL1. Biochem. Biophys. Res. Commun. 413, 420-425 CrossRef PubMed
    • (2011) Biochem. Biophys. Res. Commun. , vol.413 , pp. 420-425
    • Jiang, S.1    Wells, C.D.2    Roach, P.J.3
  • 27
    • 84890203542 scopus 로고    scopus 로고
    • Regulation of proteasome activity in health and disease
    • CrossRef PubMed
    • Schmidt, M. and Finley, D. (2014) Regulation of proteasome activity in health and disease. Biochim. Biophys. Acta 1843, 13-25 CrossRef PubMed
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 13-25
    • Schmidt, M.1    Finley, D.2
  • 28
  • 29
    • 17644444332 scopus 로고    scopus 로고
    • Laforin, the dual-phosphatase responsible for Lafora disease, interacts with R5 (PTG), a regulatory subunit of protein phosphatase-1 that enhances glycogen accumulation
    • DOI 10.1093/hmg/ddg340
    • Fernandez-Sanchez, M. E., Criado-Garcia, O., Heath, K. E., Garcia-Fojeda, B., Medrano-Fernandez, I., Gomez-Garre, P., Sanz, P., Serratosa, J. M. and Rodríguez de Córdoba, S. (2003) Laforin, the dual-phosphatase responsible for Lafora disease, interacts with R5 (PTG), a regulatory subunit of protein phosphatase-1 that enhances glycogen accumulation. Hum. Mol. Genet. 12, 3161-3171 CrossRef PubMed (Pubitemid 37508887)
    • (2003) Human Molecular Genetics , vol.12 , Issue.23 , pp. 3161-3171
    • Fernandez-Sanchez, M.E.1    Criado-Garcia, O.2    Heath, K.E.3    Garcia-Fojeda, B.4    Medrano-Fernandez, I.5    Gomez-Garre, P.6    Sanz, P.7    Serratosa, J.M.8    Rodriguez De, C.S.9
  • 30
    • 77952466937 scopus 로고    scopus 로고
    • Starch: Its metabolism, evolution, and biotechnological modification in plants
    • CrossRef PubMed
    • Zeeman, S. C., Kossmann, J. and Smith, A. M. (2010) Starch: its metabolism, evolution, and biotechnological modification in plants. Annu. Rev. Plant Biol. 61, 209-234 CrossRef PubMed
    • (2010) Annu. Rev. Plant Biol. , vol.61 , pp. 209-234
    • Zeeman, S.C.1    Kossmann, J.2    Smith, A.M.3
  • 31
    • 2942737274 scopus 로고    scopus 로고
    • Laforin preferentially binds the neurotoxic starch-like polyglucosans, which form in its absence in progressive myoclonus epilepsy
    • DOI 10.1093/hmg/ddh130
    • Chan, E. M., Ackerley, C. A., Lohi, H., Ianzano, L., Cortez, M. A., Shannon, P., Scherer, S. W. and Minassian, B. A. (2004) Laforin preferentially binds the neurotoxic starch-like polyglucosans, which form in its absence in progressive myoclonus epilepsy. Hum. Mol. Genet. 13, 1117-1129 CrossRef PubMed (Pubitemid 38786994)
    • (2004) Human Molecular Genetics , vol.13 , Issue.11 , pp. 1117-1129
    • Chan, E.M.1    Ackerley, C.A.2    Lohi, H.3    Ianzano, L.4    Cortez, M.A.5    Shannon, P.6    Scherer, S.W.7    Minassian, B.A.8
  • 34
    • 33749620777 scopus 로고    scopus 로고
    • Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates
    • DOI 10.1074/jbc.M606117200
    • Worby, C. A., Gentry, M. S. and Dixon, J. E. (2006) Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates. J. Biol. Chem. 281, 30412-30418 CrossRef PubMed (Pubitemid 44582097)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.41 , pp. 30412-30418
    • Worby, C.A.1    Gentry, M.S.2    Dixon, J.E.3
  • 36
  • 38
    • 42949086604 scopus 로고    scopus 로고
    • Malin decreases glycogen accumulation by promoting the degradation of protein targeting to glycogen (PTG)
    • CrossRef PubMed
    • Worby, C. A., Gentry, M. S. and Dixon, J. E. (2008) Malin decreases glycogen accumulation by promoting the degradation of protein targeting to glycogen (PTG). J. Biol. Chem. 283, 4069-4076 CrossRef PubMed
    • (2008) J. Biol. Chem. , vol.283 , pp. 4069-4076
    • Worby, C.A.1    Gentry, M.S.2    Dixon, J.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.